Q9SBQ7 (METK3_PETHY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
S-adenosylmethionine synthase 3
Short name=AdoMet synthase 3
EC=2.5.1.6

Alternative name(s):
Methionine adenosyltransferase 3
Short name=MAT 3

Gene names

Name:

SAM3

Organism

Petunia hybrida (Petunia)

Taxonomic identifier

4102 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Petunioideae › Petunia

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme By similarity.
Catalytic activity	ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine.
Cofactor	Binds 2 divalent ions per subunit. Magnesium or cobalt By similarity. Binds 1 potassium ion per subunit By similarity.
Pathway	Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the AdoMet synthase family.

Ontologies

Keywords
Biological process	One-carbon metabolism
Cellular component	Cytoplasm
Ligand	ATP-binding Cobalt Magnesium Metal-binding Nucleotide-binding Potassium
Molecular function	Transferase
Gene Ontology (GO)
Biological process	S-adenosylmethionine biosynthetic process Inferred from electronic annotation. Source: InterPro one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW methionine adenosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 393	393	S-adenosylmethionine synthase 3		PRO_0000363035
Regions
	Nucleotide binding	119 – 124	6	ATP Potential
	Nucleotide binding	267 – 274	8	ATP Potential
Sites
	Metal binding	17	1	Magnesium By similarity
	Metal binding	43	1	Potassium By similarity
	Metal binding	271	1	Potassium By similarity
	Metal binding	279	1	Magnesium By similarity
	Binding site	147	1	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9SBQ7 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 0AC0DD62F28F6749	FASTA	393	43,169
	10 20 30 40 50 60 METFLFTSES VNEGHPDKLC DQISDAVLDA CLEQDPESKV ACETCTKTNL VMVFGEITTK 70 80 90 100 110 120 ANVDYEKIVR DTCRNIGFIS DDVGLDADNC KVLVYIEQQS PDIAQGVHGH LTKQPEEIGA 130 140 150 160 170 180 GDQGHMFGYA TDETPEFMPL SHVLATKLGA RLTEVRKNGT CPWLRPDGKT QVTVEYYNEN 190 200 210 220 230 240 GAMVPVRVHT VLISTQHDET VTNDEIAHDL KEHVIKPVIP EKYLDEKTIF HLNPSGRFVI 250 260 270 280 290 300 GGPHGDAGLT GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYIVRQAA KSVVANGLAR 310 320 330 340 350 360 RCIVQVSYAI GVPEPLSVFV DTYGTGMIPD KEILKIVKEN FDFRPGMIAI NLDLKRGGNG 370 380 390 RFLKTAAYGH FGRDDTDFTW EVVKPLKCEK AQD

References

[1]	"Nucleotide sequence of a cDNA encoding type I S-adenosyl-L-methionine synthetase from Petunia hybrida." Hsu Y.-H., To K.-Y. Plant Gene Register PGR99-160 Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Violet. Tissue: Corolla.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF170798 mRNA. Translation: AAD48485.1.
3D structure databases
HSSP	HSSP built from PDB template 1QM4 based on UniProtKB P13444.
ProteinModelPortal	Q9SBQ7.
SMR	Q9SBQ7. Positions 3-387.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR022631. ADOMET_SYNTHASE_CS. IPR022630. S-AdoMet_synt_C. IPR022629. S-AdoMet_synt_central. IPR022628. S-AdoMet_synt_N. IPR002133. S-AdoMet_synthetase. IPR022636. S-AdoMet_synthetase_sfam. [Graphical view]
PANTHER	PTHR11964. S-AdoMet_synt. 1 hit.
Pfam	PF02773. S-AdoMet_synt_C. 1 hit. PF02772. S-AdoMet_synt_M. 1 hit. PF00438. S-AdoMet_synt_N. 1 hit. [Graphical view]
PIRSF	PIRSF000497. MAT. 1 hit.
SUPFAM	SSF55973. S-AdoMet_synt. 3 hits.
TIGRFAMs	TIGR01034. MetK. 1 hit.
PROSITE	PS00376. ADOMET_SYNTHASE_1. 1 hit. PS00377. ADOMET_SYNTHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

METK3_PETHY

Accession

Primary (citable) accession number: Q9SBQ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	May 1, 2000
Last modified:	June 28, 2011
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program